RTPR_LACAC
ID RTPR_LACAC Reviewed; 744 AA.
AC Q5FMX8;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Adenosylcobalamin-dependent ribonucleoside-triphosphate reductase;
DE Short=RTPR;
DE EC=1.17.4.2;
GN Name=rtpR; OrderedLocusNames=LBA0041;
OS Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=272621;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700396 / NCK56 / N2 / NCFM;
RX PubMed=15671160; DOI=10.1073/pnas.0409188102;
RA Altermann E., Russell W.M., Azcarate-Peril M.A., Barrangou R., Buck B.L.,
RA McAuliffe O., Souther N., Dobson A., Duong T., Callanan M., Lick S.,
RA Hamrick A., Cano R., Klaenhammer T.R.;
RT "Complete genome sequence of the probiotic lactic acid bacterium
RT Lactobacillus acidophilus NCFM.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:3906-3912(2005).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-
CC triphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-
CC triphosphate; Xref=Rhea:RHEA:12701, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:61557, ChEBI:CHEBI:61560; EC=1.17.4.2;
CC -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Allosterically regulated by ATP and dNTP.
CC {ECO:0000250}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class II ribonucleoside-triphosphate
CC reductase family. {ECO:0000305}.
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DR EMBL; CP000033; AAV41946.1; -; Genomic_DNA.
DR RefSeq; WP_003549289.1; NC_006814.3.
DR RefSeq; YP_192977.1; NC_006814.3.
DR AlphaFoldDB; Q5FMX8; -.
DR SMR; Q5FMX8; -.
DR STRING; 272621.LBA0041; -.
DR PRIDE; Q5FMX8; -.
DR EnsemblBacteria; AAV41946; AAV41946; LBA0041.
DR GeneID; 56941656; -.
DR KEGG; lac:LBA0041; -.
DR PATRIC; fig|272621.13.peg.39; -.
DR eggNOG; COG0209; Bacteria.
DR HOGENOM; CLU_002384_0_0_9; -.
DR OMA; FHCNLAE; -.
DR BioCyc; LACI272621:G1G49-39-MON; -.
DR Proteomes; UP000006381; Chromosome.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:InterPro.
DR GO; GO:0008998; F:ribonucleoside-triphosphate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR InterPro; IPR040763; RNR_alpha_hel.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013345; RTP_Rdtase_AdoCbl-dep.
DR Pfam; PF02867; Ribonuc_red_lgC; 1.
DR Pfam; PF17975; RNR_Alpha; 1.
DR TIGRFAMs; TIGR02505; RTPR; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme; Cobalamin; Cobalt; Disulfide bond; DNA replication;
KW Oxidoreductase; Redox-active center; Reference proteome.
FT CHAIN 1..744
FT /note="Adenosylcobalamin-dependent ribonucleoside-
FT triphosphate reductase"
FT /id="PRO_0000326536"
FT REGION 148..159
FT /note="Effector region-1"
FT /evidence="ECO:0000250"
FT REGION 169..318
FT /note="Effector region-2"
FT /evidence="ECO:0000250"
FT REGION 570..631
FT /note="Adenosylcobalamin-binding-1"
FT /evidence="ECO:0000250"
FT REGION 690..729
FT /note="Adenosylcobalamin-binding-2"
FT /evidence="ECO:0000250"
FT ACT_SITE 413
FT /evidence="ECO:0000250"
FT ACT_SITE 415
FT /evidence="ECO:0000250"
FT DISULFID 120..424
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 744 AA; 83521 MW; 4D3564C885BB1EB0 CRC64;
MSSTRIELDQ DFIDQVKHEI KPHWGELGWV TYKRTYARWL PEKNRSENWD ETVKRVIEGN
VNLDPRLQGT PSEEVINELT NEAKQLFRLT YGLSATPSGR NLWISGTDYQ KRTGDSLNNC
WFIAIRPQEY GDSHIVPTYI DKREKAVSMP FSFLFDQLMK GGGVGFSVVN SNIKQIPKVD
NKIDLTVVIN KSSKSHDASI KVGAVDKDEW EKQNPDHDDI IYYRLPDTRE GWVLANARLI
DMHFNNTNPD QKTKLVLDIS DIRPYGAKIH GFGGTASGPM PLVEMFIDIN NVINARVGKN
LTAVDATDIC NLIGKTVVAG NVRRSAELAL GSNDDQDFIK MKQDKEKLYH HRWASNNSVA
INSKFNNYGP IADGILHNGE PGIVNLDLSR NYGRIVDGYQ PGIDDDVEGT NPCGEISLAN
GEPCNLFEVF PYTAEKQGWN LKEAFTLATR FAKRVTFSHY DWEVSRKIIQ KNRRIGVSMS
GIQDWLLNDL GHRVVTGFED AVDEQSGEKI KKPIYDPKGI EMVDSLYKAV ITADKAYSEE
LGVNPSIKHT TVKPSGTVAK LAGVSEGMHF HYAGYLIQRI RFQASDPLLP ALKECGYHTE
PDIYTKNTIC VEFPLRAAHA DSKNFASAGT VSIEEQFATQ AFLQTYWSDN AVSCTITFQS
DENDEIAPLL RQYRHTIKST SLLPYYGGSL KQAPKEPINK KTYEERAALI TDDVEEVFTK
QNDDQKGLEL VGQTDCEGGA CPIK